Research workbench
Structure of the catalytic domain of protein tyrosine phosphatase sigma in the sulfenic acid form
Analyse Structure of the catalytic domain of protein tyrosine phosphatase sigma in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BPC
- Type
- protein
- Length
- 567 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase S
- EC
- 3.1.3.48
- UniProt
- Q13332
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase S (EC 3.1.3.48) | protein | 567 | 37% helix, 23% strand | Q13332 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 403 | 0.76 | 0.86 | 42 | empty |
| 2 | 223 | 0.56 | 0.78 | 23 | empty |
| 3 | 164 | 0.48 | 0.77 | 21 | empty |
| 4 | 121 | 0.43 | 0.77 | 23 | empty |
| 5 | 113 | 0.43 | 0.77 | 21 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 4BPC · Structure of the Catalytic Domain of Protein Tyrosine Phosphatase Sigma in the Sulfenic… · the same entry in another collection · chain A against A, TM-score 1.00
- Q13332 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase S… · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q13332
- Elsewhere: RCSB PDB 4BPC · PDBe 4BPC · UniProt Q13332
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